It has been believed until only very recently that bacteria in general do not glycosylate their proteins. While there have been some instances reported, these were dismissed as unusual anomalies (Borman 2006). It is now becoming more accepted that bacteria do glycosylate their proteins in perhaps more ways than eukaryotes do, although this belief is not yet widespread (Schäffer et al. 2001). In a recent review article, it was stated that glycosylation has been shown to assist in protein stability, modulate physical properties such as solubility, protect against proteolysis, modify activity profiles, and target for externalization (Upreti et al. 2003). In 1994, a group purified an amylase from Alicyclobacillus acidocaldarius and showed that the amylase was cell-bound, non-glycosylated and insoluble during active growth (Schwerman et al. 1994). As the culture entered stationary phase, the cells released several soluble glycosylated versions of the amylase into the medium (Schwerman et al. 1994). No attempt was made to compare the activities of the various forms of the amylases.